ID A0A0B3RPL1_9RHOB Unreviewed; 533 AA.
AC A0A0B3RPL1; A0A225PVA7; A0A225QH08;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=KU6B_51350 {ECO:0000313|EMBL:BBU58870.1}, OA50_02111
GN {ECO:0000313|EMBL:KHQ53085.1};
OS Mameliella alba.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mameliella.
OX NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ53085.1, ECO:0000313|Proteomes:UP000030960};
RN [1] {ECO:0000313|EMBL:KHQ53085.1, ECO:0000313|Proteomes:UP000030960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ53085.1,
RC ECO:0000313|Proteomes:UP000030960};
RA Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBU58870.1, ECO:0000313|Proteomes:UP000501194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KU6B {ECO:0000313|EMBL:BBU58870.1,
RC ECO:0000313|Proteomes:UP000501194};
RA Iwaki H.;
RT "Complete genome sequence of Mameliella alba strain KU6B, a
RT cyclohexylamine-degrading marine bacterium.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878,
CC ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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DR EMBL; AP022337; BBU58870.1; -; Genomic_DNA.
DR EMBL; JSUQ01000008; KHQ53085.1; -; Genomic_DNA.
DR RefSeq; WP_043140770.1; NZ_QAOY01000005.1.
DR AlphaFoldDB; A0A0B3RPL1; -.
DR STRING; 561184.SAMN05216376_106106; -.
DR GeneID; 66501289; -.
DR KEGG; malu:KU6B_51350; -.
DR PATRIC; fig|1515334.3.peg.2126; -.
DR OrthoDB; 9793626at2; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000030960; Unassembled WGS sequence.
DR Proteomes; UP000501194; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04902; ACT_3PGDH-xct; 1.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR029009; ASB_dom_sf.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000030960};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 6..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 329..446
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
SQ SEQUENCE 533 AA; 57121 MW; 35EE34AD39951F87 CRC64;
MTAPKVLVSD KLSETAVQIF RDRGIDVDFL PDVGKDKEKL AEIIGQYDGL AIRSATKVTP
SILEHAHKLK VVGRAGIGTD NVDKEAASKK GVIVMNTPFG NMITTAEHAI AMMFACARQI
PEASASTHAG KWEKSKFMGV ELTGKTLGVI GAGNIGGIVC DRARGLKMKV VAYDPFLSEE
KAGKMQVEKV EDLDDLLKRA DFITLHVPLT DQTRNILSKE NLAKTKKGVR IINCARGGLV
DEAALAELIK SGHVAGAAFD VFAEEPAKEN PLFNLPNVVC TPHLGASTSE AQENVALQVA
EQMSDYLLTG AVQNALNMPS VTAEEAKVMG PWIKLADHLG SFIGQMTDEA IKAINILYDG
EAATMNLEAL NCSLIAGIMK SVNPEVNMVS APMVARERGI KISTTNQEQS GAFEGYIKVT
VVTEKRERSI AGTVFSDGKP RFIQIKGINI DAEVGRHMLY TTNNDEPGII GALGHTMGKN
GVNIANFTLG RKDAGGEAIA LLYVDEPVPA EARAQLAETG LFNQIKPLQF DVA
//
